MCES2_ARATH
ID MCES2_ARATH Reviewed; 354 AA.
AC Q5HZ60; Q67Y41; Q682G2; Q9SUY4;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=mRNA cap guanine-N7 methyltransferase 2;
DE EC=2.1.1.56;
DE AltName: Full=mRNA (guanine-N(7))-methyltransferase 2;
DE AltName: Full=mRNA cap methyltransferase 2;
GN OrderedLocusNames=At3g52210; ORFNames=F4F15.320, T25B15.21;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: mRNA capping methyltransferase that methylates the N7
CC position of the added guanosine to the 5'-cap structure of mRNAs. Binds
CC RNA containing 5'-terminal GpppC (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA +
CC S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-
CC triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:67008, Rhea:RHEA-COMP:17166, Rhea:RHEA-
CC COMP:17167, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461,
CC ChEBI:CHEBI:167617; EC=2.1.1.56; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU00895};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q5HZ60-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5HZ60-2; Sequence=VSP_021576;
CC Name=3;
CC IsoId=Q5HZ60-3; Sequence=VSP_021577, VSP_021578;
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC site. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be due to a competing acceptor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. mRNA cap 0 methyltransferase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00895}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB41341.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL049711; CAB41341.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL132972; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002686; AEE78914.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78915.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78916.1; -; Genomic_DNA.
DR EMBL; AK175405; BAD43168.1; -; mRNA.
DR EMBL; AK176609; BAD44372.1; -; mRNA.
DR EMBL; AK176627; BAD44390.1; -; mRNA.
DR EMBL; BT020464; AAW38965.1; -; mRNA.
DR EMBL; BT020571; AAW78590.1; -; mRNA.
DR PIR; T49100; T49100.
DR RefSeq; NP_001030843.1; NM_001035766.2. [Q5HZ60-3]
DR RefSeq; NP_001030844.1; NM_001035767.2. [Q5HZ60-2]
DR RefSeq; NP_190789.3; NM_115081.4. [Q5HZ60-1]
DR AlphaFoldDB; Q5HZ60; -.
DR SMR; Q5HZ60; -.
DR STRING; 3702.AT3G52210.3; -.
DR PaxDb; Q5HZ60; -.
DR PRIDE; Q5HZ60; -.
DR ProteomicsDB; 238849; -. [Q5HZ60-1]
DR DNASU; 824386; -.
DR EnsemblPlants; AT3G52210.1; AT3G52210.1; AT3G52210. [Q5HZ60-1]
DR EnsemblPlants; AT3G52210.2; AT3G52210.2; AT3G52210. [Q5HZ60-3]
DR EnsemblPlants; AT3G52210.3; AT3G52210.3; AT3G52210. [Q5HZ60-2]
DR GeneID; 824386; -.
DR Gramene; AT3G52210.1; AT3G52210.1; AT3G52210. [Q5HZ60-1]
DR Gramene; AT3G52210.2; AT3G52210.2; AT3G52210. [Q5HZ60-3]
DR Gramene; AT3G52210.3; AT3G52210.3; AT3G52210. [Q5HZ60-2]
DR KEGG; ath:AT3G52210; -.
DR Araport; AT3G52210; -.
DR TAIR; locus:2083765; AT3G52210.
DR eggNOG; ENOG502QR4R; Eukaryota.
DR HOGENOM; CLU_045607_0_0_1; -.
DR InParanoid; Q5HZ60; -.
DR OMA; YLDEMEW; -.
DR OrthoDB; 1390749at2759; -.
DR PhylomeDB; Q5HZ60; -.
DR PRO; PR:Q5HZ60; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q5HZ60; baseline and differential.
DR GO; GO:0005845; C:mRNA cap binding complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; IBA:GO_Central.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR004971; mRNA_G-N7_MeTrfase_dom.
DR InterPro; IPR039753; RG7MT1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR12189; PTHR12189; 1.
DR Pfam; PF03291; Pox_MCEL; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51562; RNA_CAP0_MT; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Methyltransferase; mRNA capping; mRNA processing;
KW Nucleus; Reference proteome; RNA-binding; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..354
FT /note="mRNA cap guanine-N7 methyltransferase 2"
FT /id="PRO_0000260152"
FT DOMAIN 1..293
FT /note="mRNA cap 0 methyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT BINDING 21
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT BINDING 61
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT BINDING 88..89
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 48
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 278
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT VAR_SEQ 60
FT /note="I -> IV (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_021576"
FT VAR_SEQ 246..250
FT /note="RAQFA -> SLQAC (in isoform 3)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_021577"
FT VAR_SEQ 251..354
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_021578"
FT CONFLICT 83
FT /note="E -> G (in Ref. 3; BAD43168)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 354 AA; 39889 MW; D6950C807B3966D5 CRC64;
MSGFVVSKPE QSHHRLFDFA KTAIINIFAH PYATVCELYC GGAPETDKWE AAPIGHYIGI
DTSSGISSVR EAWESQRKNY DVEFFEADPS KDDFEIQLQK KLEQADLVSC WRHLQLCFET
EESARRLLTN VACLLKPGGY FFGITPDSST IWAKYQKNVE AYHNRSGAKP NVFPNYIRSE
SYMITFELEE EKFPLFGKRY QLKFSGDNAS EDHCLVHFPS LIRLAREAGL EFVEIQSLTD
FYDDNRAQFA SLLMNAGPNF VDPRGKLLPR AFDLLGLYAT FIFQKPDPDI EPPLTTPIPF
ESSNNHDERE LPVITVITDA SAPAEDPSQG LGKIVEQKGI LGPGPADLRF SEAI
